ID   SYM_UREPA               Reviewed;         521 AA.
AC   Q9PQU6;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01228};
DE            EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_01228};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01228};
DE            Short=MetRS {ECO:0000255|HAMAP-Rule:MF_01228};
GN   Name=metG {ECO:0000255|HAMAP-Rule:MF_01228}; Synonyms=metS;
GN   OrderedLocusNames=UU197;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC       also for the initiation of all mRNA translation through initiator
CC       tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_01228}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC         methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC         Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01228};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01228};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01228};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01228}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2A subfamily. {ECO:0000255|HAMAP-Rule:MF_01228}.
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DR   EMBL; AF222894; AAF30604.1; -; Genomic_DNA.
DR   RefSeq; WP_006688946.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQU6; -.
DR   SMR; Q9PQU6; -.
DR   STRING; 273119.UU197; -.
DR   EnsemblBacteria; AAF30604; AAF30604; UU197.
DR   GeneID; 29672640; -.
DR   KEGG; uur:UU197; -.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_4_14; -.
DR   OMA; SDMHGTP; -.
DR   Proteomes; UP000000423; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43326; PTHR43326; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..521
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139261"
FT   MOTIF           14..24
FT                   /note="'HIGH' region"
FT   MOTIF           306..310
FT                   /note="'KMSKS' region"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT   BINDING         309
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   521 AA;  60831 MW;  F9CD1A428B132DC5 CRC64;
     MLKQKKFFIS TPIYYSSGNP HIGHAYTTII ADVLARYKRL FGYDVFFLTG MDEHGQKIQQ
     KAFEENISPK ALVDRNSIIF LNLWKRLNIS FSKFIRTTQM DHEESVQKVF SYLYKQGKIY
     LGQWTGYYCV SCEENYNPAE IIKSQDNIML CRMGHKLETK SEESYFYKMS DQAPFLKTYY
     QNHPNFIIPN ERANEMVNNF LNNLEDLSIS RTTFDWGIPI AENPKHVIYV WLDALMNYLT
     ATGYLSNNEE LFQKYWCDNE TEIVHLLSKE IARFHCIYWP IFLNDLQIRF PSTILSHGWI
     ITKEGKMSKS LGNVIDPNVL IDTYGVDALR YYLMADLSLF RDAIFSEDNL IETYNTQLAN
     SYGNMISRTL GMLKKYRNNI VPKYVGCVLK NDEKLENLIN KNIELVQENI NKYSIDKALN
     CIQEILVEAN KYIEDNKPWE LAKNQQEQEL DSLLVHLVKV IQVTTTLLSP ILIEGSKKAV
     EQLNFDESFL TLASLASYDI FNYHKVNDSK PIFARIIVEK Q